ID ATM_YARLI Reviewed; 2282 AA.
AC Q6CAD2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 01-MAY-2013, entry version 67.
DE RecName: Full=Serine/threonine-protein kinase TEL1;
DE EC=2.7.11.1;
DE AltName: Full=ATM homolog;
DE AltName: Full=DNA-damage checkpoint kinase TEL1;
DE AltName: Full=Telomere length regulation protein 1;
GN Name=TEL1; OrderedLocusNames=YALI0D03888g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Serine/threonine protein kinase which activates
CC checkpoint signaling upon genotoxic stresses such as ionizing
CC radiation (IR), ultraviolet light (UV), or DNA replication
CC stalling, thereby acting as a DNA damage sensor. Recognizes the
CC substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to
CC form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the
CC regulation of DNA damage response mechanism. Required for the
CC control of telomere length and genome stability (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SUBUNIT: Associates with DNA double-strand breaks (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome,
CC telomere (By similarity). Note=Localizes to nuclear DNA repair
CC foci with other DNA repair proteins in response to DNA double
CC strand breaks (By similarity).
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC -!- SIMILARITY: Contains 1 FAT domain.
CC -!- SIMILARITY: Contains 1 FATC domain.
CC -!- SIMILARITY: Contains 1 PI3K/PI4K domain.
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DR EMBL; CR382130; CAG80568.1; -; Genomic_DNA.
DR RefSeq; XP_502380.1; XM_502380.1.
DR ProteinModelPortal; Q6CAD2; -.
DR GeneID; 2910592; -.
DR KEGG; yli:YALI0D03888g; -.
DR eggNOG; COG5032; -.
DR KO; K04728; -.
DR OrthoDB; EOG4VX5D9; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016572; P:histone phosphorylation; IEA:InterPro.
DR GO; GO:0090399; P:replicative senescence; IEA:InterPro.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 1.10.1070.11; -; 2.
DR InterPro; IPR015519; ATM/Tel1.
DR InterPro; IPR003152; FATC.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR014009; PIK_FAT.
DR PANTHER; PTHR11139:SF3; PTHR11139:SF3; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Kinase_like; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chromatin regulator; Chromosome; Complete proteome;
KW DNA damage; DNA repair; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Telomere;
KW Transferase.
FT CHAIN 1 2282 Serine/threonine-protein kinase TEL1.
FT /FTId=PRO_0000227707.
FT DOMAIN 1325 1844 FAT.
FT DOMAIN 1965 2282 PI3K/PI4K.
FT DOMAIN 2250 2282 FATC.
SQ SEQUENCE 2282 AA; 256251 MW; 8BC1704D61DAAC42 CRC64;
MVIRGVCDSI SRDIASSAVT GKRHTTQMSI FKTIARGHGR FKARSSRQFI VSTVCELLLA
RHKDRGSQLI VASNLRLVLS HKPHLEHLLW DHYRRSVACL CRELSALCVN SMEESGLEML
IQELLLCLDL LTKPKYVGMA ELKHDLWNCI DSMLYKYKEV SEMHVLILSI SVSLFQVVFG
SDYEICHEMV PSIFAIGTKL FTSKSKAVRE ISLRFLLKME IYLASIFGKT CPVPLDQDRL
NQIEDHMVEL LQVLKNEYNS SSLQDNDVVF EDEIVLVNSK KTMQFLICKL IAMLEYVLSY
TLTDGNVKQE EDLHGPRKKP RVSISPETPT LNAISAQIQA FQASKPISEV DKPLASLLSS
ISGSLDKTTR WKFFSAAKLL AQSPPLSPKN AHDVVFLTKW WTEGVAKLRT RSEDSACVLL
TTILRQHSSA LDPKLVVSLA SNAESKGPLK YSNVSLEFVT CASQFLISHK ACSQSQWSDW
LFVVLASEQI GATSSKMMLD TAGLLLASVG CLIRMIETPQ NTLETTTSSI MWKTDFKTTS
STSGDIELTE CMPSITIRDL KSGFQNYLNE LGDWCESASI DVNVVLPSTV FALVVCAVLD
RQGTPVGLNS RISDFLAVVT KRVEGGSCDS HVFFEAITLI NRLRHYNLLG DSLCILWDSF
INGIEKLLNV SQVTENEFDP DSPSGKNIMP DLRLSLLLRG PLKSEPFLLA IFPSDIKQYA
SCDPGKRLPE LFRYVGQTLL SSYLWDCSPL AKQLVVDLLD VYFKSGMTES SDADDLQRWV
SRDKFLVGPQ LLYGLMQVST PSEYLNLYSS VAICAAERVS SQDSYHCMDA TLTRMSSAKS
KSRLVVEEMI VALLSVHREC LSLLPVVIER VKTDMLRQKL DTDSESLVRF CKQTGTDSIL
DKILSVKVGS CVFEEEGHFS TQQLLCSEDS LQWNTQGPPL DILSRTWPDY SPCTLLMLVR
GLLNLMLKPR VSFEVPLRLV QLKYVLCLFP KRDLCSPDNY VLQQMVSCLI SFLSHSTVGA
SVRHLLSELF EVIKLPHLEG YIADLGEQSF FGADVSQLLY LLHPSEPHLC KYIEWVNSGF
SDPEAFLSVF LHTEISDKLK ATLLKSLDFG VTNMTLLGLM DIVCTKETVS FIKRASKLYS
FDWEESRVLS LLLGRGYLLF GESSNSAPKT NTETSFWNAL TSEFLTLLRG SDFTAKFAVE
VCLSKIVTKV QVQVPAELQH VFDSGVLEYT HTDEPTTGWV QKTTLELLGL LGGDFELLIP
LVRTLSSTSP LLPFIFKWTC LEYCRQGEPS YLSQILSQNS SLVVIETFFF VNSFTAHRTL
NWQPEIVNSA LTLHLYTEAL YFLEADKACW ASQEIQPSYY DIYQNIDDPD LFYGLKFTPC
LESALKQLNH ENQNLTCFEY ESGLFDWSVE TGGGESKTDI LSHLSTSGMN GLAYTINSDD
VYRWKLGLLE DPILETGTDD QTVLSQLRSI VVDEKPVLKS TLSDKYLGMQ YLLYQMQLDA
NSDYLDRIQP PDGVLDILQF CASAWRTIKT ETASYNGILT LSKLGAVSRE LNNAQISKNC
AVSLQELSRT ASHISGNVCA ISIASCLWSE AAVSRTTPVE MLKRMLGSIN PGQSPVLASQ
FCQATVLLTD WSSQARMMSP EKIHRLYIAG ASEYMALIPA GNPKTRMFHV FAKFCETQLH
SQNYDEQIHN AVMDIERLEG ELANLSRISM TREIKHAQRI SRKSLDRAKE SKLNYERLKA
MFLDSAVQFY LLSCAVRDSE YHEDVTRLIS LWFGNSHVNF VNERMQDYAL IPSFKLAPLI
NQLSSKLSYE PNNYFQTLLL DLVSATCKAH PFHCLYQISS LMRTDASPQT ERRIQAAVKV
WNTVKTQEKT ICRAMEIFTD KCVELANAEW PGKGQKASIN QFPNGSWWQN GLRKLNIPPP
TAQIPLSLDY TDIPSMNKVL AQVIKAGGIS HPKIMDFQLS DGSVSKALLK GGKDDMRQDA
IMEQVFCRVN QYFLGDPETR KRGLSIRTYN VVPMGPRAGM IEFVANTESL QAALVPLHEK
DDWDYLTGRT KMSAVAKESN SRRVEVLEEI YTHVTPVMSQ YFFQNFRSSA QAWFKARTNY
VRSAAASSML GYILGIGDRH CNNIMIDYKT GQLVHIDLGI SFDQGKNLTV PEKVPFRLTR
DMVDAMGSVG VDGPFRRCCE LSLGLFREQQ DNILSILNVL RYDPLYSWTM SPKKKQTRSS
SGSDLSDIKL EESNVTADMC LSGVKGKLAV RLSTEAVVRE LIGEAVSVEN LAVIFHGWTP
FY
//
